8f1e

Cryo-EM structure of Kap114 bound to Gsp1 (RanGTP) and H2A-H2B

Method: ELECTRON MICROSCOPY Dmax: 122.0 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Importin subunit beta-5

Saccharomyces cerevisiae S288C

UniProt P53067

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1004 Not recorded Histone H2A.2 × 1 (P04912) Histone H2B.2 × 1 (P02294) GTP-binding nuclear protein GSP1/CNR1 × 1 (P32835) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB5_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1004; UniProt 1–1004

Histone H2A.2

Saccharomyces cerevisiae S288C

UniProt P04912

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–132 Not recorded Importin subunit beta-5 × 1 (P53067) Histone H2B.2 × 1 (P02294) GTP-binding nuclear protein GSP1/CNR1 × 1 (P32835) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–131; UniProt 2–132

Histone H2B.2

Saccharomyces cerevisiae S288C

UniProt P02294

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–131 Not recorded Importin subunit beta-5 × 1 (P53067) Histone H2A.2 × 1 (P04912) GTP-binding nuclear protein GSP1/CNR1 × 1 (P32835) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 2–131

GTP-binding nuclear protein GSP1/CNR1

Saccharomyces cerevisiae S288C

UniProt P32835

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–179 Not recorded Importin subunit beta-5 × 1 (P53067) Histone H2A.2 × 1 (P04912) Histone H2B.2 × 1 (P02294) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSP1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–179; UniProt 1–179

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8f1e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f1e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f1e
Deposition date deposition_date2022-11-04
Structure title titleCryo-EM structure of Kap114 bound to Gsp1 (RanGTP) and H2A-H2B
Keywords keywords;Karyopherin Beta, Nuclear Transport, GTPase, Histone Chaperone, Histones, PROTEIN TRANSPORT-STRUCTURAL PROTEIN-NUCLEAR PROTEIN complex ;; PROTEIN TRANSPORT/STRUCTURAL PROTEIN/NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier38.15
Radius of gyration Rg (electron density) rg_electron37.63
Forward intensity I(0) i0296507000.00
Molecular weight molecular_weight144560.0 kDa
Excluded volume excluded_volume183110 ų
Envelope volume envelope_volume249220 ų
Hydration-shell volume shell_volume54490 ų
Envelope diameter envelope_diameter119.1
Shell Rg shell_rg44.82
Envelope Rg envelope_rg36.59
Shape Rg shape_rg37.62
Total Rg total_rg38.12
Total atoms total_atoms10174
Residues n_residues1273
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax122.0
Rg (real space) rg_real37.99
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real2.9650e+08
I(0) uncertainty (real space) i0_real_error5.3570e+06
Rg (reciprocal space) rg_reciprocal38.10
I(0) (reciprocal space) i0_reciprocal296500000.0000
Solution quality estimate total_estimate0.9063
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.6
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.624
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49440000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)